Aldehyde dehydrogenases active sites

Aldehyde dehydrogenases (EC 1.2.1.3 and EC 1.2.1.5) are enzymes which oxidize
a wide variety of aliphatic and aromatic aldehydes. In mammals at least four
different forms of the enzyme are known [1]: class-1 (or Ald C) a tetrameric
cytosolic enzyme, class-2 (or Ald M) a tetrameric mitochondrial enzyme, class-3 (or Ald D) a dimeric cytosolic enzyme, and class IV a microsomal enzyme.
Aldehyde dehydrogenases have also been sequenced from fungal and bacterial
species. A number of enzymes are known to be evolutionary related to aldehyde
dehydrogenases; these enzymes are listed below.

Plants and bacterial βine-aldehyde dehydrogenase (EC 1.2.1.8) [2], an
enzyme that catalyzes the last step in the biosynthesis of βine.

26G, a garden pea protein of unknown function which is induced by
dehydration of shoots [8].

Mammalian formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) [9]. This is a
cytosolic enzyme responsible for the NADP-dependent decarboxylative
reduction of 10-formyltetrahydrofolate into tetrahydrofolate. It is an
protein of about 900 amino acids which consist of three domains; the C-
terminal domain (480 residues) is structurally and functionally related to
aldehyde dehydrogenases.

Yeast hypothetical protein YBR006w.

Yeast hypothetical protein YER073w.

Yeast hypothetical protein YHR039c.

Caenorhabditis elegans hypothetical protein F01F1.6.

A glutamic acid and a cysteine residue have been implicated in the catalytic
activity of mammalian aldehyde dehydrogenase. These residues are conserved in
all the enzymes of this family. We have derived two patterns for this family,
one for each of the active site residues.

Note:

Omega-crystallins are minor structural components of squids and octopi
eye lens. They are evolutionary related to aldehyde dehydrogenases but have
lost their catalytic activity. These patterns will not detect them.

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